QUESTION 14 Match pairs of terms together that have the same value b. 1 micromole 1 μmole/l 1 mM 1 nmole a. c. d. a. 1 x 10-6 M b. 1 µmole/ml C. 1 x 10-6 moles -6 mmoles d. 1 x 10
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- Serum blood of a patient with dislipoproteinemia type 1 has milky appearance even in fasting. If serum stays at low temperature (40) for several hours fatty layer appears on its surface. What are the possible causes of these symptoms? To explain this, answer the questions and do the following tasks: a) what compounds of serum must be tested for that patient in biochemical lab? b) write the reaction which does not occur properly in patient’s blood; c) write down the schemes, explaining how the products of the previous reaction are used in adipose tissue and heart in healthy person 2 hours after a meal.Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure enzyme activity. Is it reasonable to assume that the reaction velocity obtained by measuring the amount of product after 30 minutes in a fixed-time assay is directly proportional to absorbance? How could you determine whether this was the case? Word limit 180 words including citation and referenceQ. You have now carried out the Somogyi Nelson determination of reducing sugars and measured the absorption spectra of Tube 9. What is the optimum wavelength you should use to monitor the Somogyi Nelson Assay why? Table 1._SOMOGYI-NELSON DTERMENATION OF REDUCING SUGARS Tube 1 2 3 4 5 6 7 8 9 10 D-Glucose (160 µg/mL), mL 0 0 0.125 0.125 0.25 0.25 0.375 0.375 0.5 0.5 H2O, mL 0.5 0.5 0.375 0.375 0.25 0.25 0.125 0.125 0 0 D-Galactose (160 µg/mL), mL - - - - - - - - - - D-Arabinose (160 µg/mL), mL - - - - - - - - - - Glucose-Galactose Mixture, mL - - - - - - - - - - Absorbance (710 nm) 0.049 0.051 0.138 0.151 0.271 0.26 0.382 0.395 0.454 0.444 Absorbance - blank 0 0 0.088 0.101 0.221 0.21 0.332 0.345 0.404 0.394 Final [Reducing sugar]…
- The initial velocity data shown in the table were obtained for an enzyme. Each assay at the indicated substrate concentration was initiated by adding enzyme to a final concentration of 0.01 nM. Derive Km, Vmax, kcat, and the specificity constant. [S] (mM) Velocity (x10^7) 0.10 0.96 0.125 1.12 0.167 1.35 0.250 1.66 0.50 2.22 1.0 2.63Explain how the Kirby-Bauer test works and what information it provides. Define minimum inhibitory concentration (MIC). Describe how the E-test works and what information it provides.200 ml of a 2% protein solution are available, containing an enzyme to be purified. Half of the sample is subjected to method A, consisting of fractionated precipitations, and 5 ml of final solution are obtained, with a protein concentration equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml is obtained, with a protein richness equal to 10 mg / ml, and with an enzymatic activity equal to 2000 U / ml. You want to know: a) Which of the methods has provided the purest enzyme. b) By which of the methods has the greatest amount of protein been obtained.
- Pyridoxal phosphate (PLP) is a coenzyme for the enzyme ornithine aminotransferase. The enzyme was purified from cells grow in PLP = deficient media as well as from cells grown in media that contained pyridoxal phosphate. The stability of the two different enzyme preparations was then measured by incubating the enzyme at 37°C for different lengths of time and then assaying for the amount of enzyme activity remaining. The following results were obtained. (a) Why does the amount of active enzyme decrease with the time of incubation? (b) Why does the amount of enzyme from the PLP deficient cells decline more rapidly?The enzymatic activity of PFK1 is generally measured by set- ting up a coupled enzyme assay system whereby aldolase, triose phos- phate isomerase, and glycerol-3-phosphate dehydrogenase are added to the assay mixture. For the latter enzyme, NADH is added and its change in concentration is readily monitored at 340 nm. Write the chain of reactions catalyzed by these enzymes using structural formulas, label substrates and products, and explain why the coupled en- zyme assay system leads to oxidation of NADH. While the chain of reac- tions is similar to those in glycolysis, there is a critical difference because of the dehydrogenase enzyme. Describe how this enzyme causes the chain of reactions to differ from those in glycolysis.a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?
- Calculate the Activity of an amylase enzyme which is diluted 1:100 times with phosphate buffer and incubated for 10 minutes at 37 degree Celsius. Given are the amount of maltose [mg] = 5.05 and the volume of enzyme used for the assay as 0.5ml.The turnover number for an enzyme is known to be 5000min-1. Given the following set of data, Substrate concentration(mM) 1, 2, 4, 6, 100, 1,000 Initial Rate(micromol/min) 167, 250, 334, 376, 498, 499 a) What is the Km of the enzyme for the substrate? (do this without using a calculator) b) What is the total amount of enzyme present in the assay?Enzyme X has a molecular weight of 48,000. It converts substrate Z into product Y. Z absorbs at 340 nm, and Y absorbs at 480 nm. A.) At what wavelength would you measure the change in absorbance to assay for enzyme X? Would the absorbance increase or decrease over time? B.)If Vmax = 60 μmol/min and you used 400 μL of a 0.1 mg/mL solution of enzyme, what is the turnover number?